2OM7

Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-bound Elongation Factors

Summary for 2OM7

• Entry DOI: 10.2210/pdb2om7/pdb
• Related: 1FNM 1WDT 1YL3 1YL4 2j00 2j01
• EMDB information: 1315
• Descriptor: Fragment of 16S rRNA (h14), p/E-tRNA, 30S ribosomal protein S12, ... (14 entities in total)
• Functional Keywords: rna-protein complex, ribosome
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 14
• Total formula weight: 404602.11

Authors

Connell, S.R.,Wilson, D.N.,Rost, M.,Schueler, M.,Giesebrecht, J.,Dabrowski, M.,Mielke, T.,Fucini, P.,Spahn, C.M.T. (deposition date: 2007-01-21, release date: 2008-01-15, Last modification date: 2023-12-27)

Primary citation

Connell, S.R.,Takemoto, C.,Wilson, D.N.,Wang, H.,Murayama, K.,Terada, T.,Shirouzu, M.,Rost, M.,Schuler, M.,Giesebrecht, J.,Dabrowski, M.,Mielke, T.,Fucini, P.,Yokoyama, S.,Spahn, C.M.
Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors.
Mol.Cell, 25:751-764, 2007

PubMed Abstract: Elongation factor G (EF-G) catalyzes tRNA translocation on the ribosome. Here a cryo-EM reconstruction of the 70S*EF-G ribosomal complex at 7.3 A resolution and the crystal structure of EF-G-2*GTP, an EF-G homolog, at 2.2 A resolution are presented. EF-G-2*GTP is structurally distinct from previous EF-G structures, and in the context of the cryo-EM structure, the conformational changes are associated with ribosome binding and activation of the GTP binding pocket. The P loop and switch II approach A2660-A2662 in helix 95 of the 23S rRNA, indicating an important role for these conserved bases. Furthermore, the ordering of the functionally important switch I and II regions, which interact with the bound GTP, is dependent on interactions with the ribosome in the ratcheted conformation. Therefore, a network of interaction with the ribosome establishes the active GTP conformation of EF-G and thus facilitates GTP hydrolysis and tRNA translocation.

PubMed: 17349960
DOI: 10.1016/j.molcel.2007.01.027

Experimental method

ELECTRON MICROSCOPY (7.3 Å)